Evidence map›Paper›PMID 28348716›Full record

ArticleThe journal of physical chemistry. C, Nanomaterials and interfaces2016

Understanding Protein Structure Deformation on the Surface of Gold Nanoparticles of Varying Size.

Karen E Woods, Y Randika Perera, Mackenzie B Davidson, Chloe A Wilks, Dinesh K Yadav, Nicholas C Fitzkee

Abstract read
In one paragraph

Article in The journal of physical chemistry. C, Nanomaterials and interfaces, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed.

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  16. Gold Nanoparticles Augment N-Terminal Cleavage and Splicing Reactions inFrontiers in bioengineering and biotechnology · 2021
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Karen E WoodsDepartment of Chemistry, Mississippi State University, Mississippi State, Mississippi 39762, United States.
Y Randika PereraDepartment of Chemistry, Mississippi State University, Mississippi State, Mississippi 39762, United States.
Mackenzie B DavidsonDepartment of Chemistry, Mississippi State University, Mississippi State, Mississippi 39762, United States.
Chloe A WilksDepartment of Chemistry, Mississippi State University, Mississippi State, Mississippi 39762, United States.
Dinesh K YadavDepartment of Chemistry, Mississippi State University, Mississippi State, Mississippi 39762, United States.
Nicholas C FitzkeeDepartment of Chemistry, Mississippi State University, Mississippi State, Mississippi 39762, United States.

Funding

Functionalized Gold Nanoparticles: Understanding the Mechanism of Protein BindingR15GM113152 · NIGMS · MISSISSIPPI STATE UNIVERSITY · PI FITZKEE, NICHOLAS C · 2015 to 2015
$339k
NIGMS NIH HHS R15 GM113152
6 · The paper itself

Abstract

Gold nanoparticles (AuNPs) have been of recent interest due to their unique optical properties and their biocompatibility. Biomolecules spontaneously adsorb to their surface, a trait that could potentially be exploited for drug targeting. Currently, it is unclear whether protein-AuNP interactions at the nanoparticle surface are dependent on nanoparticle size. In this work, we investigate whether varying surface curvature can induce protein unfolding and multilayer binding in citrate-coated AuNPs of various sizes. A recently developed NMR-based approach was utilized to determine the adsorption capacity, and protein NMR spectra were compared to determine whether nanoparticle size influences protein interactions at the surface. In addition, transmission electron microscopy (TEM) and dynamic light scattering (DLS) were employed to corroborate the NMR studies. Over a broad range of AuNP sizes (14-86 nm), we show that adsorption capacity can be predicted by assuming that proteins are compact and globular on the nanoparticle surface. Additionally, roughly one layer of proteins is adsorbed regardless of AuNP size. Our results hold for two proteins of significantly different sizes, GB3 (6 kDa) and bovine carbonic anhydrase (BCA, 29 kDa). However, the unstable drkN SH3 domain (Δ

Identifiers

PMID28348716
PMCPMC5365237

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.